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Figure 9.
Figure 9. (a) Solid surface (1.4 Å radius) of six
residues likely to be involved in N-type VSCC binding
interactions. These are numbered according to (1) Tyr13 (from
MVIIA), (2) Arg10 (MVIIA), (3) Leu11 (MVIIA), (4) Arg21 (MVIIA),
(5) Tyr22 (GVIA), and (6) Lys24 (GVIA). The backbone of MVIIA
(pink) is shown in correct orientation for binding. In (b), (c)
and (d) the same surface as in (a) is shown, but in dot format.
Inside this surface is shown the heavy atoms of (b) MVIIA, (c)
GVIA (backbone blue), and (d) MVIIC (backbone purple). The
side-chains are color-coded in the following manner: yellow
(hydrophobic), green (polar), red (negative) and blue
(positive). Binding surfaces which are optimally filled are
labeled in pink. Residues that form a possible clash (negative
interaction) are denoted in red (site 5 and R9 of MVIIC).
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